Purification and characterization of interferons, both human and animal, have been studied extensively over the past two decades, and the subject has been reviewed recently by Stewart in "Interferons and Their Actions," William E. Stewart II Editor, CRC Press, Inc., Cleveland, Ohio, 1977, pages 49-72. Jankowski et al, Biochemistry 15, 5182-5187 (1976), studied the binding of human interferons to Blue Dextran, i.e., dextran substituted with Cibacron Blue F3G-A, immobilized on cyanogen bromide-activated agarose. Both human fibroblast and leukocyte interferons bind to Cibacron Blue F3G-A under appropriate solvent conditions. This binding results in a significant purification of fibroblast interferon and reveals the molecular heterogeneity of human leukocyte interferon. Fibroblast interferon is reportedly eluted from the column with ethylene glycol solution, e.g., 50%, to give an 800-fold purification with a 95% recovery of activity. Similar purifications to those previously reported by Davey et al, Biochemistry 15, 704 (1976) on concanavalin A-agarose and by Sulkowski et al, J. Biol. Chem. 251, 5381 (1976) on L-tryptophan-agarose were obtained. However, the fibroblast interferon preparations employed as starting materials usually contained fetal calf serum.
Bollin et al, Preparative Biochemistry, 8, 259-274 (1978), studied binding of mouse, hamster, rabbit, horse and human fibroblast interferons on immobilized Cibacron Blue F3G-A under appropriate solvent conditions. Of the three forms of immobilized ligand investigated, interferons were most tightly bound to Blue Sepharose CL-6B, and human fibroblast interferon was displaced from the sorbant only upon inclusion of ethylene glycol in the eluant.
Erickson et al, Interferon Scientific Memoranda, March, 1979, disclose the purification of human leukocyte and human lymphoblastoid interferons in albumin-containing preparations by adsorption chromatography on Blue Sepharose.
In none of the aforementioned references was serum-free interferon employed.